The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Photo Lynn Kamerlin

Lynn Kamerlin

Professor

Photo Lynn Kamerlin

The role of ligand-gated conformational changes in enzyme catalysis

Author

  • Cátia Moreira
  • Ana Rita Calixto
  • John P Richard
  • Shina Caroline Lynn Kamerlin

Summary, in English

Structural and biochemical studies on diverse enzymes have highlighted the importance of ligand-gated conformational changes in enzyme catalysis, where the intrinsic binding energy of the common phosphoryl group of their substrates is used to drive energetically unfavorable conformational changes in catalytic loops, from inactive open to catalytically competent closed conformations. However, computational studies have historically been unable to capture the activating role of these conformational changes. Here, we discuss recent experimental and computational studies, which can remarkably pinpoint the role of ligand-gated conformational changes in enzyme catalysis, even when not modeling the loop dynamics explicitly. Finally, through our joint analyses of these data, we demonstrate how the synergy between theory and experiment is crucial for furthering our understanding of enzyme catalysis.

Publishing year

2019-10-31

Language

English

Pages

1449-1460

Publication/Series

Biochemical Society Transactions

Volume

47

Issue

5

Document type

Journal article review

Publisher

Portland Press

Keywords

  • Catalysis
  • Computer Simulation
  • Enzymes/metabolism
  • Ion Channel Gating
  • Ligands
  • Protein Conformation

Status

Published

ISBN/ISSN/Other

  • ISSN: 0300-5127